Description
Key facts
Detection method:Fluorescent,
Sample types:Inhibitor compounds,
Assay type:Quantitative,
Assay Platform:Microplate reader
Product details:
Cathepsin L Inhibitor Screening Kit (Fluorometric) (197012) is an assay that uses the ability of active Cathepsin L to cleave the synthetic AFC-based peptide substrate to release AFC, which can be easily quantified using a fluorometer or fluorescence microplate reader. In the presence of a Cathepsin L inhibitor, the cleavage of this substrate is reduced/abolished resulting in decrease or total loss of the AFC fluorescence. This simple and high-throughput adaptable assay kit can be used to screen/study/characterize potential inhibitors of Cathepsin L.
This product is manufactured by BioVision, an Abcam company and was previously called K161 Cathepsin L Inhibitor Screening Kit (Fluorometric). K161-100 is the same size as the 100 test size of ab197012.
Cathepsin L (CTSL, EC 3.4.22.15) is a lysosomal cysteine protease that is implicated in protein degradation, arthritis, apoptosis, and cancer. Cathepsin L plays a major role in antigen processing, tumor invasion and metastasis, bone resorption, and turnover of intracellular and secreted proteins involved in growth regulation. Although commonly recognized as a lysosomal protease, cathepsin L is also secreted. This broad-spectrum protease is potent in degrading several extracellular proteins (laminins, fibronectin, collagens I and IV, elastin, and other structural proteins of basement membranes) as well as serum proteins and cytoplasmic and nuclear proteins.
The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Storage information-Please refer to protocols
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Cathepsin L also known as major excreted protein (MEP) or EC 3.4.22.15 is a critical cysteine protease with a molecular weight of approximately 30-40 kDa. It performs proteolytic functions within the lysosomes executing the breakdown of proteins into peptides. This protease expresses prominently in various tissues including liver kidney spleen and lungs where it fulfills tasks integral to cellular maintenance and turnover.
Biological function summary
This protease contributes to antigen processing and the degradation of intracellular proteins. Cathepsin L participates in essential processes such as protein catabolism and the remodeling of the extracellular matrix. Although it is not part of a large protein complex its enzymatic activity influences multiple cellular functions making it an active agent in maintaining cellular homeostasis.
Pathways
Cathepsin L takes part in the antigen processing and presentation pathway contributing to immune system functions. It also associates with the lysosomal pathway for protein degradation interacting with other cathepsins such as Cathepsin B and Cathepsin D. These pathways place it centrally in maintaining protein balance within cells and its activity can affect various downstream cellular processes.
Cathepsin L has associations with cancer and neurodegenerative disorders. Its overexpression can lead to increased invasiveness and metastasis in various cancers due to enhanced proteolytic activity. It also relates to Alzheimer's disease where abnormal protease function can disrupt the processing of amyloid precursor protein contributing to amyloid beta aggregation. In these conditions cathepsin L functions in concert with proteins like Cathepsin B linking it to pathological processes.
